ID A0A3G1TJ06_LEICE Unreviewed; 346 AA. AC A0A3G1TJ06; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 03-JUL-2019, entry version 4. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00093744}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS01109717}; GN Name=ND2 {ECO:0000313|EMBL:AYC44947.1}; OS Leiothlypis celata orestera. OG Mitochondrion {ECO:0000313|EMBL:AYC44947.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Parulidae; Leiothlypis. OX NCBI_TaxID=2320902 {ECO:0000313|EMBL:AYC44947.1}; RN [1] {ECO:0000313|EMBL:AYC44947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZRH173 {ECO:0000313|EMBL:AYC44947.1}; RA Hanna Z.R., Cicero C., Bowie R.C.K.; RT "Phylogeography of the orange-crowned warbler (Oreothlypis celata; RT Aves: Passeriformes: Parulidae)."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone. {ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS00093760}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=7.1.1.2; Evidence={ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS01125045}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00387338}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003403, CC ECO:0000256|SAAS:SAAS00387338}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00573211}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MG686781; AYC44947.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro. DR InterPro; IPR010933; NADH_DH_su2_C. DR InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF06444; NADH_dehy_S2_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01436; NADHDHGNASE2. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093681}; KW Membrane {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464716}; KW Mitochondrion {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093699, ECO:0000313|EMBL:AYC44947.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093736}; KW NAD {ECO:0000256|RuleBase:RU003403, ECO:0000256|SAAS:SAAS00464384}; KW Respiratory chain {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464594}; KW Translocase {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS01109684}; KW Transmembrane {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464491}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00093666}; KW Transport {ECO:0000256|SAAS:SAAS00464711}; KW Ubiquinone {ECO:0000256|RuleBase:RU003403, KW ECO:0000256|SAAS:SAAS00464648}. FT TRANSMEM 5 21 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 56 75 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 95 115 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 152 171 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 178 196 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 202 222 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 242 261 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 281 304 Helical. {ECO:0000256|RuleBase:RU003403}. FT TRANSMEM 325 345 Helical. {ECO:0000256|RuleBase:RU003403}. FT DOMAIN 23 288 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 290 343 NADH_dehy_S2_C. {ECO:0000259|Pfam: FT PF06444}. SQ SEQUENCE 346 AA; 38289 MW; 439E9253E9DA052C CRC64; MNPQANLIFI ISLLLGTTIT ISSNHWIMAW TGLEINTLAI LPLISKSHHP RAIEAATKYF LTQAAASALV LFSSMTNAWH TGQWDITQLT HPTSSLILTS AIAMKLGLVP FHFWFPEVLQ GSPLTTGLLL STMMKLPPIT LLYMTSPSLN PTLLTTLAIL STALGGWMGL NQTQIRKILA FSSISHLGWM AIIIIYNPKL TLLNFYLYAM MTTTVFLTLN TIKVLKLSTL MTAWTKIPSL NAMLLLTLLS LAGLPPLTGF LPKWLIIQEL TKQDMAPAAT LISLLSLLSL FFYLRLAYCT TITLPPHTTN HMKQWRTNKS TNITIAILTT MSVMLLPISP MILTIV //